Introduction: Exploring post-translational modifications (PTMs) with the use of mass
spectrometry (PTMomics) is a rapidly developing area, with methods for discovery …

Protein phosphorylation on serine, threonine, and tyrosine is well established as a crucial
regulatory posttranslational modification in eukaryotes. With the recent whole‐genome …

Abstract dbPTM is a database that compiles information on protein post-translational
modifications (PTMs), such as the catalytic sites, solvent accessibility of amino acid residues …

The term 'exoproteome'describes the protein content that can be found in the extracellular
proximity of a given biological system. These proteins arise from cellular secretion, other …

We set out to provide a resource to the microbiology community especially with respect to
systems biology based endeavors. To this end, we generated a comprehensive dataset …

We are all colonized by a large microbiome, a complex set of microbes that have intimate
associations with us. Culture-based approaches have provided insights in the complexity of …

Even though protein initiator methionine excision (NME) and N-terminal acetylation (NTA)
have been relatively well investigated in eukaryotic proteomes, few studies were dedicated …

Over the past decade, liquid chromatography coupled with tandem mass spectrometry (LC–
MS/MS) has evolved into the main proteome discovery technology. Up to several thousand …

Post-translational modifications (PTMs) can occur soon after translation or at any stage in
the lifecycle of a given protein, and they may help regulate protein folding, stability, cellular …

Increasing evidence shows that protein phosphorylation on serine, threonine and tyrosine
residues is a major regulatory post-translational modification in the bacteria. This review …